ID B3PHR2_CELJU Unreviewed; 1260 AA.
AC B3PHR2;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=CJA_3654 {ECO:0000313|EMBL:ACE85108.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85108.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE85108.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85108.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000934; ACE85108.1; -; Genomic_DNA.
DR RefSeq; WP_012489228.1; NC_010995.1.
DR AlphaFoldDB; B3PHR2; -.
DR STRING; 498211.CJA_3654; -.
DR KEGG; cja:CJA_3654; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3283; Bacteria.
DR eggNOG; COG3447; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_68_6; -.
DR OrthoDB; 6187449at2; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACE85108.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW Transferase {ECO:0000313|EMBL:ACE85108.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 49..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 549..619
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 622..674
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 746..798
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 816..1031
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1055..1170
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 532..559
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1104
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1260 AA; 140500 MW; 9639578C051B3D40 CRC64;
MDLLRLTDSL PLPQSLRLLL LNLVLVLAYL ALAKFGLGWS SLTTDVTLIW PAAGLALFSI
MTFGLRAAPG VLIGSASTTL LLHFNQQDVP LGPESLLATL AMSSADLLQV VLIAKLNSQL
LLRNSPIRSR RVLFFIGCVL LCCVFSASVG VVSLYQLGLL NLGTLPENWL TWWMGDCIGM
LVFTPLLAWA LLPGLRHQDA RAQAFLLLSS GLGVLLLLVA TLGYLERSAA RDRFEGESNL
LWLALSTRLS GSLHDLDLAQ HNITLGGASD REFLRLARSL LEHNPWLNHI AWVPTQAGEQ
LEPSLAALNL GDSQMVTRHS TRITRAKLAL GHPGNRTVIL NAWQQRELRA GPVYYGERGR
PALEIYSPVM TCPSEQPCSL RGLLSAQLNL TEWASQAFSP ELPDQLQLLL VTGGPDPLRL
QWQPGGWVDA SPDSNQPVAH LRYQRSLPLA DQTMEMITYH QNPLWFVPSW LQVSTLGIGL
ALISLLSAYL ITRQKHQDLL MRNQSRLQEE IHISTQALRK ANDWLLKEVE QRQQTQEQLE
SSQEVLRRRE QELRSLLDNI PDPIWLKDIE GHYLNCNRAF AQLLGKTEQE IVGKREHELV
SADIAQVFRR NDRVALGSAG PHRHEQWLVA ADGRLHMLDT LKVAVRDADN QTYGILGIGR
DITDKHELIS ELEKFKRFAE FSAQGFGIAS LKGETLYMNP SMRRMLSDRS TNEDDFKQQF
WLYYPPELQV RVRDDIFPKV VEQGHWQGEL AALHADGSDF PTQETFFVIR DDQGKPQYIG
NVMTDISAQK ETEAELSQAK EAAEEAARAK SRFLANMSHE IRTPLNAVLG YTQLLMRDPQ
LAGNQRERLQ LILNASQRLL GLINDVLDLS KIESGALNLR QDYFDLHQEM QEIHAIIAER
ANAKGLSLGL EIDFPAPNIV RGDRQKLGQI LLNLLGNAVK FTHQGSVNLM LTRHGDWVDF
VISDTGPGIA PQELEQLFSA FRQGQAGQDS GGTGLGLTLS RHLAQGMGGS LELTSQLGEG
TRAHLRLPLP SEALTRHNSD KPNTIVRLAP GSHCHVLVVE DDQASADVLV SLLEQLGCTT
RCAYNGREGI DWCAQERFDI IFTDIRMPDV NGLEMLRQLR RQADFVTPLV AVSASSLEHE
RTYYLAQGFH DFIGKPYGFE EIFSALQQHS GARFEAPEPA PSQPLVYQDD PINFNLAGQS
LQQIRQTAAS GDMSLCKKLA NQLSADLLGQ QRHQQLLAAI KQYDLERVEA LVNSWLDGSR
//
